Molecular dynamics simulations of Factor Xa: insight into conformational transition of its binding subsites.
Molecular dynamics simulations of Factor Xa: insight into conformational transition of its binding subsites.
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Xa 因子的分子动力学模拟：深入了解其结合亚位点的构象转变。
DOI：
10.1002/bip.21062
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发表时间：
2008
期刊：
影响因子：
2.9
通讯作者：
Briggs,JamesM
中科院分区：
文献类型：
--
作者：
Singh,Narender;Briggs,JamesM
众所周知，蛋白质的柔性和构象多样性是许多蛋白质功能的关键特征。人凝血蛋白具有多种底物，并且需要各种蛋白质-蛋白质相互作用以使凝血级联的平稳功能维持血液止血。为了解决蛋白质如何科普与其结构多样的底物的多重相互作用以及可能驱动这些变化的伴随结构变化，我们研究了人类因子X。我们采用了20纳秒的分子动力学（MD）和操纵分子动力学（SMD）模拟两种不同的构象形式的因子X，开放和关闭，并观察到一个可互换的构象转变从一个到另一个。这项工作也证明了各种芳香族残基参与芳香族-芳香族相互作用的作用，这使得这种动态转变成为可能。© 2008 Wiley Periodicals，Inc. Biopolymers 89：1104-1113，2008。这篇文章最初作为公认的预印本在线发表。“在线发布”日期对应于预印本。您可以通过向Biopolymers编辑部发送电子邮件（biopolymers@wiley.com）索取预印本的副本
Protein flexibility and conformational diversity is well known to be a key characteristic of the function of many proteins. Human blood coagulation proteins have multiple substrates, and various protein–protein interactions are required for the smooth functioning of the coagulation cascade to maintain blood hemostasis. To address how a protein may cope with multiple interactions with its structurally diverse substrates and the accompanied structural changes that may drive these changes, we studied human Factor X. We employed 20 ns of molecular dynamics (MD) and steered molecular dynamics (SMD) simulations on two different conformational forms of Factor X, open and closed, and observed an interchangeable conformational transition from one to another. This work also demonstrates the roles of various aromatic residues involved in aromatic–aromatic interactions, which make this dynamic transition possible. © 2008 Wiley Periodicals, Inc. Biopolymers 89: 1104–1113, 2008.This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com